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Protein

Pyridoxal phosphate phosphatase PHOSPHO2

Gene

Phospho2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Phosphatase that has high activity toward pyridoxal 5'-phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate (By similarity).By similarity

Catalytic activityi

Pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81NucleophileBy similarity
Metal bindingi8 – 81MagnesiumBy similarity
Active sitei10 – 101Proton donorBy similarity
Metal bindingi10 – 101MagnesiumBy similarity
Binding sitei19 – 191SubstrateBy similarity
Binding sitei99 – 991SubstrateBy similarity
Metal bindingi179 – 1791MagnesiumBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxal phosphate phosphatase PHOSPHO2 (EC:3.1.3.74)
Gene namesi
Name:Phospho2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1920623. Phospho2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Pyridoxal phosphate phosphatase PHOSPHO2PRO_0000068834Add
BLAST

Proteomic databases

EPDiQ9D9M5.
MaxQBiQ9D9M5.
PaxDbiQ9D9M5.
PeptideAtlasiQ9D9M5.
PRIDEiQ9D9M5.

Expressioni

Gene expression databases

BgeeiQ9D9M5.
CleanExiMM_PHOSPHO2.
ExpressionAtlasiQ9D9M5. baseline and differential.
GenevisibleiQ9D9M5. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028494.

Structurei

3D structure databases

ProteinModelPortaliQ9D9M5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3120. Eukaryota.
ENOG4111NAQ. LUCA.
GeneTreeiENSGT00390000007741.
HOGENOMiHOG000231038.
HOVERGENiHBG080058.
InParanoidiQ9D9M5.
KOiK13248.
OMAiLLVWKSG.
PhylomeDBiQ9D9M5.
TreeFamiTF300112.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006383. HAD-SF_hydro_IB_PSP-like.
IPR016965. Pase_PHOSPHO-typ.
IPR006384. PyrdxlP_Pase-rel.
[Graphical view]
PfamiPF06888. Put_Phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF031051. PyrdxlP_Pase_PHOSPHO2. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01489. DKMTPPase-SF. 1 hit.
TIGR01488. HAD-SF-IB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9D9M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVLLVFDFD NTIIDDNSDT WIVQCAPDKK LPIELQDSYQ KGLWTEFMGR
60 70 80 90 100
VFKYLRDEGV KADELKRAVT SLPFTSGMIE LLSFLRMNKD RFDCIIISDS
110 120 130 140 150
NSIFIDWVLE AAAFHDVFDH VFTNPASFDS SGRLTVKNYH AHSCTRCPKN
160 170 180 190 200
LCKNTVLGEF IDKQLQKGVR YTRIVYIGDG GNDVCPVTFL KKNDVAMPRE
210 220 230 240
GYTLHRTLAK MSQNLEPMES SIVVWSSGVE IISHLQFLIK M
Length:241
Mass (Da):27,563
Last modified:June 1, 2001 - v1
Checksum:i9E0036C310AD26BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861P → Q in BAE21125 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006724 mRNA. Translation: BAB24714.1.
AK132362 mRNA. Translation: BAE21125.1.
AK159551 mRNA. Translation: BAE35176.1.
AL845261 Genomic DNA. Translation: CAM16374.1.
BC025612 mRNA. Translation: AAH25612.1.
BC031523 mRNA. Translation: AAH31523.1.
CCDSiCCDS16099.1.
RefSeqiNP_082797.1. NM_028521.2.
XP_006500320.1. XM_006500257.1.
XP_011238097.1. XM_011239795.1.
UniGeneiMm.9621.

Genome annotation databases

EnsembliENSMUST00000028494; ENSMUSP00000028494; ENSMUSG00000027088.
ENSMUST00000112266; ENSMUSP00000107885; ENSMUSG00000027088.
ENSMUST00000180290; ENSMUSP00000136471; ENSMUSG00000027088.
GeneIDi73373.
KEGGimmu:73373.
UCSCiuc008jyp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006724 mRNA. Translation: BAB24714.1.
AK132362 mRNA. Translation: BAE21125.1.
AK159551 mRNA. Translation: BAE35176.1.
AL845261 Genomic DNA. Translation: CAM16374.1.
BC025612 mRNA. Translation: AAH25612.1.
BC031523 mRNA. Translation: AAH31523.1.
CCDSiCCDS16099.1.
RefSeqiNP_082797.1. NM_028521.2.
XP_006500320.1. XM_006500257.1.
XP_011238097.1. XM_011239795.1.
UniGeneiMm.9621.

3D structure databases

ProteinModelPortaliQ9D9M5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028494.

Proteomic databases

EPDiQ9D9M5.
MaxQBiQ9D9M5.
PaxDbiQ9D9M5.
PeptideAtlasiQ9D9M5.
PRIDEiQ9D9M5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028494; ENSMUSP00000028494; ENSMUSG00000027088.
ENSMUST00000112266; ENSMUSP00000107885; ENSMUSG00000027088.
ENSMUST00000180290; ENSMUSP00000136471; ENSMUSG00000027088.
GeneIDi73373.
KEGGimmu:73373.
UCSCiuc008jyp.1. mouse.

Organism-specific databases

CTDi493911.
MGIiMGI:1920623. Phospho2.

Phylogenomic databases

eggNOGiKOG3120. Eukaryota.
ENOG4111NAQ. LUCA.
GeneTreeiENSGT00390000007741.
HOGENOMiHOG000231038.
HOVERGENiHBG080058.
InParanoidiQ9D9M5.
KOiK13248.
OMAiLLVWKSG.
PhylomeDBiQ9D9M5.
TreeFamiTF300112.

Miscellaneous databases

PROiQ9D9M5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D9M5.
CleanExiMM_PHOSPHO2.
ExpressionAtlasiQ9D9M5. baseline and differential.
GenevisibleiQ9D9M5. MM.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006383. HAD-SF_hydro_IB_PSP-like.
IPR016965. Pase_PHOSPHO-typ.
IPR006384. PyrdxlP_Pase-rel.
[Graphical view]
PfamiPF06888. Put_Phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF031051. PyrdxlP_Pase_PHOSPHO2. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01489. DKMTPPase-SF. 1 hit.
TIGR01488. HAD-SF-IB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Testis.

Entry informationi

Entry nameiPHOP2_MOUSE
AccessioniPrimary (citable) accession number: Q9D9M5
Secondary accession number(s): A2AR04, Q3V1M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.